GT-CORE (public beta v1)

Glycosyltransferase Curated Online Resource for Enzymology

Family-organised sequence, structure, mechanism and substrate-specificity records for the CAZy glycosyltransferases

earP

Neisseria meningitidis serogroup B / serotype 15 (strain H44/76) · Protein-arginine rhamnosyltransferase (EC 2.4.1.-)

GT104Non-model organism · annotation 4–5Fold GT-BInverting5 PDB structure(s)

External resources

Identification and annotation

CAZy familyGT104 · CAZy entry
Gene symbolearP
Synonyms / alternate namesEF-P arginine rhamnosyltransferase
UniProt accessionE6MVV9
NCBI Gene IDnot curated
Source speciesNeisseria meningitidis serogroup B / serotype 15 (strain H44/76)
Taxonomic domainBacteria
UniProt annotation level4

Function and localisation

Enzyme functionProtein-arginine rhamnosyltransferase (EC 2.4.1.-)
Subcellular locationnot curated

Structure and mechanism

Fold typeGT-B
Catalytic mechanismInverting
Cation dependenceNo
Oligomeric statenot curated
PDB structures5WXI, 5WXJ, 5WXK, 5XVR, 7VCH

Donor and acceptor specificity

Sugar nucleotide donordTDP-beta-L-rhamnose
Donor CCD code(s)not curated
Acceptor substrate(s)L-arginyl-[protein]
Acceptor CCD / GlycoCTnot curated

Protein sequences

Full protein sequence

382 aa
MNTPPFVCWIFCKVIDNFGDIGVSWRLARVLHRELGWQVHLWTDDVSALRALCPDLPDVPCVHQDIHVRTWHSDAADIDTAPVPDVVIETFACDLPENVLHIIRRHKPLWLNWEYLSAEESNERLHLMPSPQEGVQKYFWFMGFSEKSGGLIRERDYCEAVRFDTEALRERLMLPEKNASEWLLFGYRSDVWAKWLEMWRQAGSPMTLLLAGTQIIDSLKQSGVIPQDALQNDGDVFQTASVRLVKIPFVPQQDFDQLLHLADCAVIRGEDSFVRAQLAGKPFFWHIYPQDENVHLDKLHAFWDKAHGFYTPETVSAHRRLSDDLNGGEALSATQRLECWQTLQQHQNGWRQGAEDWSRYLFGQPSAPEKLAAFVSKHQKIR

Catalytic domain sequence

366 aa
IFCKVIDNFGDIGVSWRLARVLHRELGWQVHLWTDDVSALRALCPDLPDVPCVHQDIHVRTWHSDAADIDTAPVPDVVIETFACDLPENVLHIIRRHKPLWLNWEYLSAEESNERLHLMPSPQEGVQKYFWFMGFSEKSGGLIRERDYCEAVRFDTEALRERLMLPEKNASEWLLFGYRSDVWAKWLEMWRQAGSPMTLLLAGTQIIDSLKQSGVIPQDALQNDGDVFQTASVRLVKIPFVPQQDFDQLLHLADCAVIRGEDSFVRAQLAGKPFFWHIYPQDENVHLDKLHAFWDKAHGFYTPETVSAHRRLSDDLNGGEALSATQRLECWQTLQQHQNGWRQGAEDWSRYLFGQPSAPEKLAAFV